Format

Send to

Choose Destination
Biomol NMR Assign. 2019 Oct;13(2):339-343. doi: 10.1007/s12104-019-09902-0. Epub 2019 Jul 1.

Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains.

Author information

1
Department of Biochemistry & Molecular Genetics, School of Medicine, University of Colorado, 12801 E. 17th Avenue, Aurora, CO, 80045, USA.
2
Department of Biochemistry & Molecular Genetics, School of Medicine, University of Colorado, 12801 E. 17th Avenue, Aurora, CO, 80045, USA. beat.vogeli@ucdenver.edu.
3
Department of Pharmaceutical Organic Chemistry, Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt.

Abstract

Olduvai protein domains, encoded primarily by NBPF genes, have been linked to both human brain evolution and cognitive diseases such as autism and schizophrenia. There are six primary domains that comprise the Olduvai family: three conserved domains (CON1-3) and three human lineage-specific domains (HLS1-3), which typically occur as a triplet (HLS1, HLS2 and HLS3). Herein, we present the solution NMR assignment of the backbone chemical shifts of the separate HLS1, 2 and 3 domains of NBPF15. Our data suggest that there is no change in the structure of the separate domains when compared to the full-length triplet (HLS1-HLS2-HLS3). We also demonstrate that there is no direct interaction between the three domains.

KEYWORDS:

Autism; Backbone chemical shift assignment; Brain evolution; DUF1220; Gene duplication; Olduvai; Protein domains; Schizophrenia

PMID:
31264103
PMCID:
PMC6715528
[Available on 2020-10-01]
DOI:
10.1007/s12104-019-09902-0
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Springer
Loading ...
Support Center